The clpP multigenic family in Streptomyces lividans: conditional expression of the clpP3 clpP4 operon is controlled by PopR, a novel transcriptional activator

Mol Microbiol. 2000 Nov;38(3):602-12. doi: 10.1046/j.1365-2958.2000.02155.x.

Abstract

The clpP genes are widespread among living organisms and encode the proteolytic subunit of the Clp ATP-dependent protease. These genes are present in a single copy in most eubacteria. However, five clpP genes were identified in Streptomyces coelicolor. The clpP1 clpP2 operon was studied: mutations affected the growth cycle in various Streptomyces. Here, we report studies of the expression of the clpP3 clpP4 operon in Streptomyces lividans. The clpP3 operon was induced in a clpP1 mutant strain, and the regulation of expression was investigated in detail. The product of the putative regulator gene, downstream from clpP4, was purified. Gel migration shift assays and DNase I footprinting showed that this protein binds to the clpP3 promoter and recognizes a tandem 6 bp palindromic repeat (TCTGCC-3N-GGCAGA). In vivo, this DNA-binding protein, named PopR, acts as an activator of the clpP3 operon. Studies of popR expression indicate that the regulator is probably controlled at the post-transcriptional level.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism*
  • Base Sequence
  • DNA-Binding Proteins / metabolism
  • Endopeptidase Clp
  • Gene Expression Regulation, Bacterial / genetics
  • Molecular Sequence Data
  • Multigene Family
  • Operon*
  • Promoter Regions, Genetic / genetics
  • Promoter Regions, Genetic / physiology
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / metabolism*
  • Streptomyces / enzymology*
  • Streptomyces / genetics
  • Trans-Activators / genetics*
  • Trans-Activators / metabolism
  • Transcription, Genetic
  • Transcriptional Activation / genetics*

Substances

  • DNA-Binding Proteins
  • Trans-Activators
  • Serine Endopeptidases
  • Endopeptidase Clp
  • Adenosine Triphosphatases